{"id":156,"date":"2024-10-28T14:37:15","date_gmt":"2024-10-28T13:37:15","guid":{"rendered":"http:\/\/wwww.icp.universite-paris-saclay.fr\/cpsysbio\/?page_id=156"},"modified":"2024-11-08T10:20:52","modified_gmt":"2024-11-08T09:20:52","slug":"nadph-oxidase","status":"publish","type":"page","link":"https:\/\/www.icp.universite-paris-saclay.fr\/cpsysbio\/en\/scientific-axes\/nadph-oxidase\/","title":{"rendered":"NADPH Oxidase"},"content":{"rendered":"

The Phagocyte NADPH Oxidase: From Cell Signaling to Molecular Mechanisms<\/h3>\n
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The NADPH oxidase present in phagocytes functions to produce superoxide anions in a controlled manner, leading to the generation of reactive oxygen species (ROS). Its activity is essential for the innate immune system to fight infections and destroy pathogens sequestered within phagosomes. The enzyme\u2019s membrane-bound subunits (Nox2, p22phox) and cytosolic subunits (p47phox, p67phox, p40phox, and Rac) are separated in resting cells and only assemble after activation of cellular signaling pathways, forming an active complex at the phagosome membrane. In this conformation, the enzyme can bind its substrate (NADPH) and facilitate transmembrane electron transfers. This spatial and temporal regulation prevents the uncontrolled generation of ROS, which could otherwise lead to harmful oxidative stress, damaging both the cells and surrounding tissues. This enzyme also plays a critical role in severe inflammatory pathologies and is currently a focus of therapeutic developments aimed at controlling its activity.<\/p>\n<\/div>\n<\/div><\/div><\/div><\/div>

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Our study models for NADPH oxidase range (from left to right) from isolated proteins to phagocytic cells, including giant unilamellar vesicles (GUVs) and model cell lines (COS7; PLB985).<\/em><\/p>\n<\/div>\n<\/div><\/div><\/div><\/div>

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Three teams within the CPSysBio group focus on this theme:<\/p>\n